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P53618

- COPB_HUMAN

UniProt

P53618 - COPB_HUMAN

Protein

Coatomer subunit beta

Gene

COPB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte surface triglyceride lipase (PNPLA2) with the lipid droplet to mediate lipolysis By similarity. Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1. Promotes degradation of Nef cellular targets CD4 and MHC class I antigens by facilitating their trafficking to degradative compartments.By similarity4 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. structural molecule activity Source: InterPro

    GO - Biological processi

    1. COPI coating of Golgi vesicle Source: Reactome
    2. intracellular protein transport Source: InterPro
    3. intra-Golgi vesicle-mediated transport Source: UniProtKB
    4. membrane organization Source: Reactome
    5. retrograde vesicle-mediated transport, Golgi to ER Source: Reactome
    6. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    ER-Golgi transport, Host-virus interaction, Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_11096. COPI Mediated Transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Coatomer subunit beta
    Alternative name(s):
    Beta-coat protein
    Short name:
    Beta-COP
    Gene namesi
    Name:COPB1
    Synonyms:COPB
    ORF Names:MSTP026
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:2231. COPB1.

    Subcellular locationi

    Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicleCOPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane. Endoplasmic reticulum-Golgi intermediate compartment
    Note: The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Proteolytic cleavage by CAPN8 triggers translocation from Golgi to cytoplasm By similarity. Found in perinuclear vesicular-tubular clusters (VTCs) and in the Golgi region where associated with vesicles, buds and rims of the Golgi stack By similarity. Occasionally present at the trans-side of Golgi, but mainly present at the cis-Golgi side in transitional areas (TA), on so-called peripheral elements (PE) consisting of tubules and vesicles located between the cup-shaped transitional elements (TE) of the rough endoplasmic reticulum (RER) and the cis-most Golgi cisternae By similarity. Present in cytoplasm, not associated with visible coats or membranes, with a minor fraction present on small clusters of tubules and vesicles By similarity. Some association with high-density and low-density microsomes and mitochondria/nuclei fraction By similarity. Very little found in plasma membrane fraction By similarity.By similarity

    GO - Cellular componenti

    1. COPI vesicle coat Source: UniProtKB
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB-SubCell
    5. Golgi apparatus Source: HPA
    6. Golgi-associated vesicle Source: ProtInc
    7. Golgi membrane Source: ProtInc
    8. intracellular membrane-bounded organelle Source: HPA
    9. membrane Source: UniProtKB
    10. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26747.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 953952Coatomer subunit betaPRO_0000193833Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine2 Publications
    Modified residuei494 – 4941N6-acetyllysineBy similarity

    Post-translational modificationi

    Proteolytically cleaved between Ser-528 and Ser-529 by CAPN8.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP53618.
    PaxDbiP53618.
    PeptideAtlasiP53618.
    PRIDEiP53618.

    PTM databases

    PhosphoSiteiP53618.

    Expressioni

    Gene expression databases

    ArrayExpressiP53618.
    BgeeiP53618.
    CleanExiHS_COPB1.
    GenevestigatoriP53618.

    Organism-specific databases

    HPAiCAB012338.
    HPA040166.
    HPA043954.

    Interactioni

    Subunit structurei

    Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Interacts (via C-terminus) with HIV-1 Nef; the interaction is direct. Interacts with SCYL1. Interacts with COPG1. Interacts (via trunk domain) with ARF1 (via switch I region); the interaction is direct. Interacts with KCNK2/TREK (via N-terminus); this interaction increases the channel-mediated whole cell currents and promotes plasma membrane expression of KCNK2/TREK. Interacts with anthrax lethal factor (LF); this interaction may facilitate endosomal vesicle membrane translocation of LF and its release from the lumen of endosomal vesicles to external milieu. Interacts with CAPN8 and PRKCE By similarity. Interacts with ARF1 (myristoylated); this interaction is required for binding of COPB1 to Golgi membranes By similarity. Interacts with STX17 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HTTP428583EBI-359063,EBI-466029
    NUDCD1Q96RS62EBI-359063,EBI-2512429
    SUN2Q9UH992EBI-359063,EBI-1044964

    Protein-protein interaction databases

    BioGridi107710. 57 interactions.
    DIPiDIP-265N.
    IntActiP53618. 34 interactions.
    MINTiMINT-1151935.
    STRINGi9606.ENSP00000249923.

    Structurei

    3D structure databases

    ProteinModelPortaliP53618.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati96 – 13136HEAT 1Add
    BLAST
    Repeati132 – 16837HEAT 2Add
    BLAST
    Repeati240 – 27637HEAT 3Add
    BLAST
    Repeati277 – 31438HEAT 4Add
    BLAST
    Repeati316 – 35338HEAT 5Add
    BLAST
    Repeati396 – 43338HEAT 6Add
    BLAST

    Sequence similaritiesi

    Contains 6 HEAT repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5096.
    HOGENOMiHOG000207417.
    HOVERGENiHBG005380.
    InParanoidiP53618.
    KOiK17301.
    OMAiVHALMEF.
    OrthoDBiEOG7ZWD12.
    PhylomeDBiP53618.
    TreeFamiTF105737.

    Family and domain databases

    Gene3Di1.25.10.10. 3 hits.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR002553. Clathrin/coatomer_adapt-like_N.
    IPR011710. Coatomer_bsu_C.
    IPR016460. COPB1.
    IPR029446. COPB1_appendage_platform_dom.
    [Graphical view]
    PANTHERiPTHR10635. PTHR10635. 1 hit.
    PfamiPF01602. Adaptin_N. 1 hit.
    PF07718. Coatamer_beta_C. 1 hit.
    PF14806. Coatomer_b_Cpla. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005727. Coatomer_beta_subunit. 1 hit.
    SUPFAMiSSF48371. SSF48371. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P53618-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTAAENVCYT LINVPMDSEP PSEISLKNDL EKGDVKSKTE ALKKVIIMIL    50
    NGEKLPGLLM TIIRFVLPLQ DHTIKKLLLV FWEIVPKTTP DGRLLHEMIL 100
    VCDAYRKDLQ HPNEFIRGST LRFLCKLKEA ELLEPLMPAI RACLEHRHSY 150
    VRRNAVLAIY TIYRNFEHLI PDAPELIHDF LVNEKDASCK RNAFMMLIHA 200
    DQDRALDYLS TCIDQVQTFG DILQLVIVEL IYKVCHANPS ERARFIRCIY 250
    NLLQSSSPAV KYEAAGTLVT LSSAPTAIKA AAQCYIDLII KESDNNVKLI 300
    VLDRLIELKE HPAHERVLQD LVMDILRVLS TPDLEVRKKT LQLALDLVSS 350
    RNVEELVIVL KKEVIKTNNV SEHEDTDKYR QLLVRTLHSC SVRFPDMAAN 400
    VIPVLMEFLS DNNEAAAADV LEFVREAIQR FDNLRMLIVE KMLEVFHAIK 450
    SVKIYRGALW ILGEYCSTKE DIQSVMTEIR RSLGEIPIVE SEIKKEAGEL 500
    KPEEEITVGP VQKLVTEMGT YATQSALSSS RPTKKEEDRP PLRGFLLDGD 550
    FFVAASLATT LTKIALRYVA LVQEKKKQNS FVAEAMLLMA TILHLGKSSL 600
    PKKPITDDDV DRISLCLKVL SECSPLMNDI FNKECRQSLS HMLSAKLEEE 650
    KLSQKKESEK RNVTVQPDDP ISFMQLTAKN EMNCKEDQFQ LSLLAAMGNT 700
    QRKEAADPLA SKLNKVTQLT GFSDPVYAEA YVHVNQYDIV LDVLVVNQTS 750
    DTLQNCTLEL ATLGDLKLVE KPSPLTLAPH DFANIKANVK VASTENGIIF 800
    GNIVYDVSGA ASDRNCVVLS DIHIDIMDYI QPATCTDAEF RQMWAEFEWE 850
    NKVTVNTNMV DLNDYLQHIL KSTNMKCLTP EKALSGYCGF MAANLYARSI 900
    FGEDALANVS IEKPIHQGPD AAVTGHIRIR AKSQGMALSL GDKINLSQKK 950
    TSI 953
    Length:953
    Mass (Da):107,142
    Last modified:October 17, 2006 - v3
    Checksum:iBE916C1C5A599D79
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti825 – 8251D → E in AAD41240. 1 PublicationCurated
    Sequence conflicti825 – 8251D → E in CAA57622. (PubMed:7982906)Curated
    Sequence conflicti847 – 8471F → L in AAD41240. 1 PublicationCurated
    Sequence conflicti847 – 8471F → L in CAA57622. (PubMed:7982906)Curated
    Sequence conflicti911 – 9111I → S in AAD41240. 1 PublicationCurated
    Sequence conflicti911 – 9111I → S in CAA57622. (PubMed:7982906)Curated
    Sequence conflicti915 – 9151I → L in AAD41240. 1 PublicationCurated
    Sequence conflicti915 – 9151I → L in CAA57622. (PubMed:7982906)Curated
    Sequence conflicti925 – 9251G → V in AAD41240. 1 PublicationCurated
    Sequence conflicti925 – 9251G → V in CAA57622. (PubMed:7982906)Curated
    Sequence conflicti950 – 9501K → E in AAD41240. 1 PublicationCurated
    Sequence conflicti950 – 9501K → E in CAA57622. (PubMed:7982906)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF084457 mRNA. Translation: AAD41240.1.
    AF111807 mRNA. Translation: AAL39009.1.
    AL136593 mRNA. Translation: CAB66528.1.
    CH471064 Genomic DNA. Translation: EAW68481.1.
    CH471064 Genomic DNA. Translation: EAW68482.1.
    CH471064 Genomic DNA. Translation: EAW68483.1.
    CH471064 Genomic DNA. Translation: EAW68484.1.
    CH471064 Genomic DNA. Translation: EAW68485.1.
    BC037280 mRNA. Translation: AAH37280.1.
    X82103 mRNA. Translation: CAA57622.1.
    CCDSiCCDS7815.1.
    PIRiA55136.
    T46913.
    RefSeqiNP_001137533.1. NM_001144061.1.
    NP_001137534.1. NM_001144062.1.
    NP_057535.1. NM_016451.4.
    UniGeneiHs.339278.

    Genome annotation databases

    EnsembliENST00000249923; ENSP00000249923; ENSG00000129083.
    ENST00000439561; ENSP00000397873; ENSG00000129083.
    GeneIDi1315.
    KEGGihsa:1315.
    UCSCiuc001mlg.2. human.

    Polymorphism databases

    DMDMi116241311.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF084457 mRNA. Translation: AAD41240.1 .
    AF111807 mRNA. Translation: AAL39009.1 .
    AL136593 mRNA. Translation: CAB66528.1 .
    CH471064 Genomic DNA. Translation: EAW68481.1 .
    CH471064 Genomic DNA. Translation: EAW68482.1 .
    CH471064 Genomic DNA. Translation: EAW68483.1 .
    CH471064 Genomic DNA. Translation: EAW68484.1 .
    CH471064 Genomic DNA. Translation: EAW68485.1 .
    BC037280 mRNA. Translation: AAH37280.1 .
    X82103 mRNA. Translation: CAA57622.1 .
    CCDSi CCDS7815.1.
    PIRi A55136.
    T46913.
    RefSeqi NP_001137533.1. NM_001144061.1.
    NP_001137534.1. NM_001144062.1.
    NP_057535.1. NM_016451.4.
    UniGenei Hs.339278.

    3D structure databases

    ProteinModelPortali P53618.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107710. 57 interactions.
    DIPi DIP-265N.
    IntActi P53618. 34 interactions.
    MINTi MINT-1151935.
    STRINGi 9606.ENSP00000249923.

    PTM databases

    PhosphoSitei P53618.

    Polymorphism databases

    DMDMi 116241311.

    Proteomic databases

    MaxQBi P53618.
    PaxDbi P53618.
    PeptideAtlasi P53618.
    PRIDEi P53618.

    Protocols and materials databases

    DNASUi 1315.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000249923 ; ENSP00000249923 ; ENSG00000129083 .
    ENST00000439561 ; ENSP00000397873 ; ENSG00000129083 .
    GeneIDi 1315.
    KEGGi hsa:1315.
    UCSCi uc001mlg.2. human.

    Organism-specific databases

    CTDi 1315.
    GeneCardsi GC11M014436.
    H-InvDB HIX0009466.
    HGNCi HGNC:2231. COPB1.
    HPAi CAB012338.
    HPA040166.
    HPA043954.
    MIMi 600959. gene.
    neXtProti NX_P53618.
    PharmGKBi PA26747.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5096.
    HOGENOMi HOG000207417.
    HOVERGENi HBG005380.
    InParanoidi P53618.
    KOi K17301.
    OMAi VHALMEF.
    OrthoDBi EOG7ZWD12.
    PhylomeDBi P53618.
    TreeFami TF105737.

    Enzyme and pathway databases

    Reactomei REACT_11096. COPI Mediated Transport.

    Miscellaneous databases

    ChiTaRSi COPB1. human.
    GeneWikii COPB1.
    GenomeRNAii 1315.
    NextBioi 5379.
    PROi P53618.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P53618.
    Bgeei P53618.
    CleanExi HS_COPB1.
    Genevestigatori P53618.

    Family and domain databases

    Gene3Di 1.25.10.10. 3 hits.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR002553. Clathrin/coatomer_adapt-like_N.
    IPR011710. Coatomer_bsu_C.
    IPR016460. COPB1.
    IPR029446. COPB1_appendage_platform_dom.
    [Graphical view ]
    PANTHERi PTHR10635. PTHR10635. 1 hit.
    Pfami PF01602. Adaptin_N. 1 hit.
    PF07718. Coatamer_beta_C. 1 hit.
    PF14806. Coatomer_b_Cpla. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005727. Coatomer_beta_subunit. 1 hit.
    SUPFAMi SSF48371. SSF48371. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Human beta-cop homolog gene, complete CDS."
      Zhang J., Liu T., Fu G., Li W., Ye M., Zhou J., Wu J., Shen Y., Yu M., Chen S., Mao M., Chen Z.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Aorta.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Amygdala.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    6. "Physical interaction of the HIV-1 Nef protein with beta-COP, a component of non-clathrin-coated vesicles essential for membrane traffic."
      Benichou S., Bomsel M., Bodeus M., Durand H., Doute M., Letourneur F., Camonis J., Benarous R.
      J. Biol. Chem. 269:30073-30076(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 651-953, INTERACTION WITH HIV-1 NEF.
      Tissue: Lymphoid tissue.
    7. "The oculocerebrorenal syndrome gene product is a 105-kD protein localized to the Golgi complex."
      Olivos-Glander I.M., Janne P.A., Nussbaum R.L.
      Am. J. Hum. Genet. 57:817-823(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    8. "Identification and characterization of novel isoforms of COP I subunits."
      Futatsumori M., Kasai K., Takatsu H., Shin H.-W., Nakayama K.
      J. Biochem. 128:793-801(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH COPG1, SUBUNIT, SUBCELLULAR LOCATION.
    9. "Multiple and stepwise interactions between coatomer and ADP-ribosylation factor-1 (Arf1)-GTP."
      Sun Z., Anderl F., Frohlich K., Zhao L., Hanke S., Brugger B., Wieland F., Bethune J.
      Traffic 8:582-593(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARF1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "Depletion of beta-COP reveals a role for COP-I in compartmentalization of secretory compartments and in biosynthetic transport of caveolin-1."
      Styers M.L., O'Connor A.K., Grabski R., Cormet-Boyaka E., Sztul E.
      Am. J. Physiol. 294:C1485-C1498(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. "Scyl1, mutated in a recessive form of spinocerebellar neurodegeneration, regulates COPI-mediated retrograde traffic."
      Burman J.L., Bourbonniere L., Philie J., Stroh T., Dejgaard S.Y., Presley J.F., McPherson P.S.
      J. Biol. Chem. 283:22774-22786(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SCYL1.
    12. "HIV-1 Nef targets MHC-I and CD4 for degradation via a final common beta-COP-dependent pathway in T cells."
      Schaefer M.R., Wonderlich E.R., Roeth J.F., Leonard J.A., Collins K.L.
      PLoS Pathog. 4:E1000131-E1000131(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HIV-1 NEF.
    13. "COPI coatomer complex proteins facilitate the translocation of anthrax lethal factor across vesicular membranes in vitro."
      Tamayo A.G., Bharti A., Trujillo C., Harrison R., Murphy J.R.
      Proc. Natl. Acad. Sci. U.S.A. 105:5254-5259(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANTHRAX LETHAL FACTOR.
    14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    15. "Early endosomes and endosomal coatomer are required for autophagy."
      Razi M., Chan E.Y., Tooze S.A.
      J. Cell Biol. 185:305-321(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Enhancement of TREK1 channel surface expression by protein-protein interaction with beta-COP."
      Kim E., Hwang E.M., Yarishkin O., Yoo J.C., Kim D., Park N., Cho M., Lee Y.S., Sun C.H., Yi G.S., Yoo J., Kang D., Han J., Hong S.G., Park J.Y.
      Biochem. Biophys. Res. Commun. 395:244-250(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KCNK2, SUBCELLULAR LOCATION.
    17. "Quantitative proteomics analysis of cell cycle-regulated Golgi disassembly and reassembly."
      Chen X., Simon E.S., Xiang Y., Kachman M., Andrews P.C., Wang Y.
      J. Biol. Chem. 285:7197-7207(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCOPB_HUMAN
    AccessioniPrimary (citable) accession number: P53618
    Secondary accession number(s): D3DQX0
    , Q6GTT7, Q9NTK2, Q9UNW7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 132 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Brefeldin A induces dissociation from the Golgi of the beta-COP and presumably the other coatomer subunits.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3